Mammalian prothymosin alpha links to tRNA in Escherichia coli cells
| Autor: | A, Vartapetian, D, Lukashev, I, Lyakhov, A, Belyaeva, N, Chichkova, A, Bogdanov |
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| Rok vydání: | 1997 |
| Předmět: |
RNA
Transfer Met Sequence Analysis RNA Molecular Sequence Data Blotting Northern Polymerase Chain Reaction Chromatography Affinity Peptide Fragments Recombinant Proteins Rats Thymosin RNA Bacterial RNA Transfer Mutagenesis Escherichia coli Animals Nucleic Acid Conformation RNA Transfer Lys Electrophoresis Polyacrylamide Gel Trypsin Amino Acid Sequence Protein Precursors hormones hormone substitutes and hormone antagonists RNA Transfer Ser Research Article |
| Zdroj: | RNA (New York, N.Y.). 3(10) |
| ISSN: | 1355-8382 |
| Popis: | Prothymosin alpha, a small and highly acidic nuclear protein related to cell proliferation, is known to be covalently attached to a small unidentified cytoplasmic RNA in mammalian cells. Here we demonstrate that recombinant rat prothymosin a links covalently to an RNA when overproduced in Escherichia coli cells. The RNA species of this complex is represented by a wide range of bacterial tRNAs. tRNA(Lys), tRNA(3Ser), tRNA(2Ile), and tRNA(mMet) were identified by sequencing. Prothymosin alpha appears to be linked to the 5' terminus of tRNA. tRNA attachment site lies close to the carboxy-terminus of prothymosin alpha. Furthermore, the carboxy-terminal peptide of prothymosin alpha is also competent for tRNA binding. The site of tRNA attachment coincides with the nuclear localization signal of prothymosin alpha, and tRNA binding might be expected to affect subcellular localization of this protein. |
| Databáze: | OpenAIRE |
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